Structure of PDB 1lwt Chain A Binding Site BS02

Receptor Information
>1lwt Chain A (length=448) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSV
VQKSQHRAHKSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYF
EVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNK
AYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTI
EGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEY
KDRKAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSF
LSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARS
LGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRP
APAAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHN
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1lwt Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence.
Resolution3.2 Å
Binding residue
(original residue number in PDB)
Q55 H56 R57 V126 S127 K128 S129 G168 S169 H170 S227 A261 N274 R277 K336 S362 N364 E366 H377 Y384
Binding residue
(residue number reindexed from 1)
Q55 H56 R57 V124 S125 K126 S127 G166 S167 H168 S225 A255 N268 R271 K330 S356 N358 E360 H371 Y378
Enzymatic activity
Catalytic site (original residue number in PDB) C1 N76 T78 H79 K301 K403 G433 I434 N454
Catalytic site (residue number reindexed from 1) C1 N74 T76 H77 K295 K397 G427 I428 N448
Enzyme Commision number 3.1.-.-
7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0004519 endonuclease activity
Biological Process
GO:0016539 intein-mediated protein splicing
GO:0030908 protein splicing

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1lwt, PDBe:1lwt, PDBj:1lwt
PDBsum1lwt
PubMed12219083
UniProtP17255|VATA_YEAST V-type proton ATPase catalytic subunit A (Gene Name=VMA1)

[Back to BioLiP]